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J Biol Chem, Vol. 273, Issue 15, 8849-8859, April 10, 1998

The Assembly System for the Lipopolysaccharide R2 Core-type of Escherichia coli Is a Hybrid of Those Found in Escherichia coli K-12 and Salmonella enterica
STRUCTURE AND FUNCTION OF THE R2 WaaK AND WaaL HOMOLOGS

David E. HeinrichsDagger , Mario A. Monteiro, Malcolm B. Perry, and Chris WhitfieldDagger

From the Dagger  Department of Microbiology, University of Guelph, Guelph, Ontario, Canada N1G 2W1 and  Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada K1A OR6

In Escherichia coli F632, the 14-kilobase pair chromosomal region located between waaC (formerly rfaC) and waaA (kdtA) contains genes encoding enzymes required for the synthesis of the type R2 core oligosaccharide portion of lipopolysaccharide. Ten of the 13 open reading frames encode predicted products sharing greater than 90% total similarity with homologs in E. coli K-12. However, the products of waaK (rfaK) and waaL (rfaL) each resemble homologs in Salmonella enterica serovar Typhimurium but share little similarity with E. coli K-12. The F632 WaaK and WaaL proteins therefore define differences between the type R2 and K-12 outer core oligosaccharides of E. coli lipopolysaccharides. Based on the chemical structure of the core oligosaccharide of an E. coli F632 waaK::aacC1 mutant and in vitro glycosyltransferase analyses, waaK encodes UDP-N-acetylglucosamine:(glucose) lipopolysaccharide alpha 1,2-N-acetylglucosaminyltransferase. The WaaK enzyme adds a terminal GlcNAc side branch substituent that is crucial for the recognition of core oligosaccharide acceptor by the O-polysaccharide ligase, WaaL. Results of complementation analyses of E. coli K-12 and F632 waaL mutants suggest that structural differences between the WaaL proteins play a role in recognition of, and interaction with, terminal lipopolysaccharide core moieties.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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